2BG9: Nicotinic acetylcholine receptor

Refined structure of the nicotinic acetylcholine receptor at 4A resolution. Determined by electron microscopy at 4.0 Å resolution. Released 16 Feb 2005.

Method: Electron microscopy
Resolution: 4.0 Å
Organism: TORPEDO MARMORATA
Chains: 5
Atoms: 14,924
Mol. weight: 211.75 kDa
Released: 16 Feb 2005

Explore 2BG9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BG9 contains 55 α-helices and 72 β-strands across 5 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 10 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
β-strand	29-44	16	1
β-strand	49-60	12	1
α-helix	72-75	4
β-strand	78-81	4	1
α-helix	82-84	3
β-strand	90-92	3	2
β-strand	100-101	2	1
β-strand	107-110	4	1
β-strand	116-118	3	1
β-strand	121-127	7	1
β-strand	140-148	9	2
β-strand	156-159	4	1
β-strand	177-187	11	2
β-strand	199-208	10	2
α-helix	213-238	26
α-helix	240-242	3
α-helix	243-270	28
α-helix	275-277	3
α-helix	278-300	23
α-helix	375-398	24
α-helix	406-435	30

Chain B: 9 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	4-14	11
β-strand	30-34	5	3
β-strand	37-44	8	4
β-strand	49-55	7	4
β-strand	57-61	5	3
β-strand	77-81	5	3
β-strand	90-92	3	5
β-strand	100-101	2	4
β-strand	107-111	5	3
β-strand	115-118	4	3
β-strand	121-126	6	4
β-strand	143-148	6	5
β-strand	153	1	6
β-strand	157-159	3	3
β-strand	187-188	2	7
β-strand	193-195	3	5
β-strand	204	1	6
β-strand	207-210	4	5
β-strand	213-214	2	7
α-helix	221-226	6
α-helix	227-231	5
α-helix	232-240	9
α-helix	248-274	27
α-helix	282-306	25
α-helix	404-429	26
α-helix	433-461	29
α-helix	463-465	3

Chain C: 10 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	4-11	8
β-strand	32-46	15	8
β-strand	51-63	13	8
α-helix	71-75	5
β-strand	80-82	3	8
α-helix	84-86	3
β-strand	92-94	3	9
β-strand	103	1	8
β-strand	110-112	3	8
β-strand	117-120	4	8
β-strand	123-128	6	8
α-helix	133-135	3
β-strand	143-150	8	9
β-strand	159-161	3	8
α-helix	180-182	3
β-strand	190-194	5	9
β-strand	197-201	5	9
β-strand	213-223	11	9
α-helix	228-253	26
α-helix	257-283	27
α-helix	289-314	26
α-helix	422-448	27
α-helix	453-479	27

Chain D: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
β-strand	30-32	3	10
β-strand	37-44	8	11
β-strand	49-55	7	11
β-strand	58-60	3	10
α-helix	63-65	3
α-helix	72-75	4
β-strand	78-81	4	12
α-helix	82-84	3
β-strand	90-92	3	13
β-strand	101	1	11
β-strand	107-110	4	12
β-strand	116-118	3	10
β-strand	121-127	7	11
β-strand	141-148	8	13
β-strand	157-159	3	10
α-helix	167-169	3
β-strand	177-187	11	13
β-strand	199-208	10	13
α-helix	213-239	27
α-helix	240-242	3
α-helix	243-270	28
α-helix	275-277	3
α-helix	278-300	23
α-helix	375-400	26
α-helix	405-435	31

Chain E: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11
β-strand	30-43	14	14
β-strand	48-60	13	14
α-helix	62-64	3
β-strand	77	1	14
α-helix	81-83	3
β-strand	89-91	3	15
β-strand	100	1	14
β-strand	108-109	2	14
β-strand	114-117	4	14
β-strand	120-125	6	14
α-helix	139	1
β-strand	140	1	16
α-helix	141	1
β-strand	143-147	5	15
β-strand	157-158	2	14
α-helix	173-175	3
β-strand	183-187	5	16
β-strand	192-193	2	15
β-strand	207-210	4	15
β-strand	213-216	4	16
α-helix	222-245	24
α-helix	248-250	3
α-helix	251-278	28
α-helix	284-306	23
α-helix	415-441	27
α-helix	444-461	18
α-helix	462-466	5
α-helix	467-473	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Acetylcholine receptor protein, alpha chain	A, D	protein	370	TORPEDO MARMORATA	P02711 (AlphaFold model)
Acetylcholine receptor protein, beta chain	B	protein	370	TORPEDO MARMORATA	Q6S3I0 (AlphaFold model)
Acetylcholine receptor protein, delta chain	C	protein	369	TORPEDO MARMORATA	Q6S3H8 (AlphaFold model)
Acetylcholine receptor protein, gamma chain	E	protein	370	TORPEDO MARMORATA	Q6S3H9 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>2BG9_1 ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN (chains A, D)
SEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLINVDEVNQIVETNVRLRQQW
IDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTP
PAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKD
YRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVVNVIIPCLLFSFLTVLVFYLPTDSG
EKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIVTVVVINTHH
RSPSTHSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFA
GRLIELSQEG

Sequence of entity 2 (B), FASTA

>2BG9_2 ACETYLCHOLINE RECEPTOR PROTEIN, BETA CHAIN (chains B)
SVMEDTLLSVLFENYNPKVRPSQTVGDKVTVRVGLTLTSLLILNEKNEEMTTSVFLNLAW
TDYRLQWDPAAYEGIKDLSIPSDDVWQPDIVLMNNNDGSFEITLHVNVLVQHTGAVSWHP
SAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEVILQHALDAMINQDAFTENGQWSIE
HKPSRKNWRSDDPSYEDVTFYLIIQRKPLFYIVYTIVPCILISILAILVFYLPPDAGEKM
SLSISALLALTVFLLLLADKVPETSLSVPIIISYLMFIMILVAFSVILSVVVLNLHHRSP
NTHEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYIFITMCSIGTFSIFLDAS
HNVPPDNPFA

Sequence of entity 3 (C), FASTA

>2BG9_3 ACETYLCHOLINE RECEPTOR PROTEIN, DELTA CHAIN (chains C)
VNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTTNVWMDH
AWYDHRLTWNASEYSDISILRLRPELIWIPDIVLQNNNDGQYNVAYFCNVLVRPNGYVTW
LPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYNANEISMDLIIDPEAFTENGEWEIIHK
PAKKNIYGDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLAALAFYLPAESGE
KMSTAICVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVVVNCGIVLNFHFR
TPSTHSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVM
GNFNRPPAK

Sequence of entity 4 (E), FASTA

>2BG9_4 ACETYLCHOLINE RECEPTOR PROTEIN, GAMMA CHAIN (chains E)
NEEGRLIEKLLGDYDKRIKPAKTLDHVIDVTLKLTLTNLISLNEKEEALTTNVWIEIQWN
DYRLSWNTSEYEGIDLVRIPSELLWLPDVVLENNVDGQFEVAYYANVLVYNDGSMYWLPP
AIYRSTCPIAVTYFPFDWQNCSLVFRSQTYNAHEVNLQLSAEEGIDPEDFTENGEWTIRH
RPAKKNYNWQLTKDDIDFQEIIFFLIIQRKPLFYIINIIAPCVLISSLVVLVYFLPAQAG
GQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSLVIVTNCVIVLNVS
LRTPNTHSCVEACNFIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSLGTLAIF
LTGHLNQVPE

Primary citation

Refined Structure of the Nicotinic Acetylcholine Receptor at 4A Resolution. Unwin, N. J Mol Biol (2005) 346:967. DOI 10.1016/J.JMB.2004.12.031 · PubMed

Other PDB entries of the same protein (UniProt P02711 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1OED 4.0 Å, Structure of acetylcholine receptor pore from electron images
4AQ5 6.2 Å, Gating movement in acetylcholine receptor analysed by time-resolved electron…
4AQ9 6.2 Å, Gating movement in acetylcholine receptor analysed by time- resolved electron…
4BON 40.0 Å, The structure and super-organization of acetylcholine receptor-rapsyn complexes class B
4BOI 41.0 Å, The structure and super-organization of acetylcholine receptor-rapsyn complexes class A
4BOO 42.0 Å, The structure and super-organization of acetylcholine receptor-rapsyn complexes class C
4BOR 42.0 Å, The structure and super-organization of acetylcholine receptor-rapsyn complexes class D
4BOT 42.0 Å, The structure and super-organization of acetylcholine receptor- rapsyn complexes class E
4BOG 50.0 Å, The structure and super-organization of acetylcholine receptor-rapsyn complexes
1L4W NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202)…
1LJZ NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202)…

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